Structure and function of fatty acid amide hydrolase.

@article{McKinney2005StructureAF,
  title={Structure and function of fatty acid amide hydrolase.},
  author={Michele K. McKinney and Benjamin F. Cravatt},
  journal={Annual review of biochemistry},
  year={2005},
  volume={74},
  pages={
          411-32
        }
}
Fatty acid amide hydrolase (FAAH) is a mammalian integral membrane enzyme that degrades the fatty acid amide family of endogenous signaling lipids, which includes the endogenous cannabinoid anandamide and the sleep-inducing substance oleamide. FAAH belongs to a large and diverse class of enzymes referred to as the amidase signature (AS) family. Investigations into the structure and function of FAAH, in combination with complementary studies of other AS enzymes, have engendered provocative… 
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Molecular Dynamics Analysis of FAAH Complexed with Anandamide
Fatty Acid Amide Hydrolase (FAAH) is a very interesting serine hydrolase that promotes the hydrolysis of both amides and esters, such as the endogenous cannabinoid anandamide or N-arachidonoyl
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TLDR
The significant changes in substrate selectivity achieved by single amino acid changes suggest that FAAH possesses a rather malleable substrate binding domain and may serve, along with other AS enzymes, as a template for the engineering of amidases with novel and/or tailored specificities.
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TLDR
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TLDR
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TLDR
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TLDR
The molecular characterization of both a mouse and a human FAAH and compare these enzymes to the rat FAAH demonstrate well conserved in primary structure and support a general role for the fatty acid amides in mammalian biology.
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TLDR
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Fatty acid amide hydrolase (FAAH) is a mammalian integral membrane enzyme responsible for the hydrolysis of a number of neuromodulatory fatty acid amides, including the endogenous cannabinoid
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